Crystal structure and biochemical investigations reveal novel mode of substrate selectivity and illuminate substrate inhibition and allostericity in a subfamily of Xaa-Pro dipeptidases

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dc.contributor.authorAre, V. N.
dc.contributor.authorAshwani Kumar
dc.contributor.authorSaurabh Kumar
dc.contributor.authorGoyal, V. D.
dc.contributor.authorGhosh, B.
dc.contributor.authorJamdar, S. N.
dc.contributor.authorMakde, R. D.
dc.date.accessioned2020-09-10T11:00:50Z
dc.date.available2020-09-10T11:00:50Z
dc.date.issued2017
dc.description.divisionHP&SRPD;FTDen
dc.format.extent4660 bytes
dc.format.mimetypetext/html
dc.identifier.sourceBiochimica et Biophysica Acta-General Subjects, 2017. Vol. 1865: pp. 153-164en
dc.identifier.urihttp://hdl.handle.net/123456789/20569
dc.language.isoenen
dc.subjectProlidaseen
dc.subjectPeptidase-Qen
dc.subjectM24B metallopeptidaseen
dc.subjectX-ray crystallographyen
dc.subjectXanthomonas campestrisen
dc.subjectMycobacterium tuberculosisen
dc.titleCrystal structure and biochemical investigations reveal novel mode of substrate selectivity and illuminate substrate inhibition and allostericity in a subfamily of Xaa-Pro dipeptidasesen
dc.typeArticleen

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